Header list of 1x5s.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 16-MAY-05 1X5S
TITLE SOLUTION STRUCTURE OF RRM DOMAIN IN A18 HNRNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COLD-INDUCIBLE RNA-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RRM DOMAIN;
COMPND 5 SYNONYM: GLYCINE-RICH RNA-BINDING PROTEIN CIRP, A18 HNRNP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CIRBP, A18HNRNP, CIRP;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040510-11;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURE GENOMICS, RRM DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.SATO,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X5S 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X5S 1 VERSN
REVDAT 1 16-NOV-05 1X5S 0
JRNL AUTH A.SATO,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RRM DOMAIN IN A18 HNRNP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.017
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X5S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024414.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM U-15,13C; 20MM PHOSPHATE
REMARK 210 BUFFER NA; 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.925, CYANA 2.017
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 ARG A 52 -70.34 -104.56
REMARK 500 1 SER A 53 126.91 -174.99
REMARK 500 1 ASN A 75 93.44 -37.11
REMARK 500 2 VAL A 32 -64.52 -93.04
REMARK 500 2 ASP A 47 179.19 -52.98
REMARK 500 2 ARG A 52 -74.62 -98.74
REMARK 500 2 SER A 53 137.15 -174.39
REMARK 500 2 ASN A 75 90.42 -54.24
REMARK 500 2 SER A 101 -49.90 -134.50
REMARK 500 3 ALA A 9 51.60 72.82
REMARK 500 3 VAL A 32 -71.44 -87.56
REMARK 500 3 ASP A 66 -34.46 -36.30
REMARK 500 3 ASN A 75 98.98 -52.91
REMARK 500 3 ARG A 96 106.65 -170.39
REMARK 500 4 SER A 2 110.66 -166.04
REMARK 500 4 VAL A 32 -72.25 -71.99
REMARK 500 4 PHE A 33 -36.92 -38.00
REMARK 500 4 ASP A 47 178.59 -54.45
REMARK 500 4 SER A 53 102.50 -40.55
REMARK 500 4 ASN A 75 101.67 -43.19
REMARK 500 4 ALA A 89 100.76 -49.89
REMARK 500 4 SER A 93 129.38 -174.61
REMARK 500 4 ASN A 95 -61.72 -98.01
REMARK 500 5 VAL A 32 -71.82 -86.34
REMARK 500 5 ARG A 52 -70.35 -93.61
REMARK 500 5 SER A 53 116.08 -175.34
REMARK 500 5 ASN A 75 98.18 -42.03
REMARK 500 5 PRO A 99 -177.35 -69.74
REMARK 500 6 MET A 8 153.32 -38.51
REMARK 500 6 SER A 21 172.36 -56.25
REMARK 500 6 VAL A 32 -64.30 -90.52
REMARK 500 6 SER A 53 100.83 -41.05
REMARK 500 6 ASN A 75 95.02 -36.80
REMARK 500 7 SER A 3 102.81 -56.89
REMARK 500 7 MET A 8 41.64 37.02
REMARK 500 7 LEU A 20 133.11 -37.21
REMARK 500 7 VAL A 32 -71.36 -76.38
REMARK 500 7 PHE A 33 -33.73 -39.51
REMARK 500 7 SER A 53 109.77 -43.10
REMARK 500 7 ASN A 75 96.11 -39.44
REMARK 500 7 SER A 97 142.86 -172.74
REMARK 500 7 PRO A 99 -177.10 -69.78
REMARK 500 8 PHE A 33 -19.87 -47.62
REMARK 500 8 SER A 40 -45.25 -130.16
REMARK 500 8 ASP A 47 172.48 -56.05
REMARK 500 8 SER A 53 103.66 -47.22
REMARK 500 8 ASN A 75 96.32 -36.76
REMARK 500 9 SER A 5 174.62 -57.16
REMARK 500 9 VAL A 32 -70.68 -79.04
REMARK 500 9 ASP A 47 167.58 -48.89
REMARK 500
REMARK 500 THIS ENTRY HAS 122 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000586.1 RELATED DB: TARGETDB
DBREF 1X5S A 8 96 UNP Q14011 CIRBP_HUMAN 1 89
SEQADV 1X5S GLY A 1 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S SER A 2 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S SER A 3 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S GLY A 4 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S SER A 5 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S SER A 6 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S GLY A 7 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S SER A 97 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S GLY A 98 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S PRO A 99 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S SER A 100 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S SER A 101 UNP Q14011 CLONING ARTIFACT
SEQADV 1X5S GLY A 102 UNP Q14011 CLONING ARTIFACT
SEQRES 1 A 102 GLY SER SER GLY SER SER GLY MET ALA SER ASP GLU GLY
SEQRES 2 A 102 LYS LEU PHE VAL GLY GLY LEU SER PHE ASP THR ASN GLU
SEQRES 3 A 102 GLN SER LEU GLU GLN VAL PHE SER LYS TYR GLY GLN ILE
SEQRES 4 A 102 SER GLU VAL VAL VAL VAL LYS ASP ARG GLU THR GLN ARG
SEQRES 5 A 102 SER ARG GLY PHE GLY PHE VAL THR PHE GLU ASN ILE ASP
SEQRES 6 A 102 ASP ALA LYS ASP ALA MET MET ALA MET ASN GLY LYS SER
SEQRES 7 A 102 VAL ASP GLY ARG GLN ILE ARG VAL ASP GLN ALA GLY LYS
SEQRES 8 A 102 SER SER ASP ASN ARG SER GLY PRO SER SER GLY
HELIX 1 1 GLU A 26 TYR A 36 1 11
HELIX 2 2 ILE A 64 MET A 74 1 11
SHEET 1 A 4 GLU A 41 VAL A 44 0
SHEET 2 A 4 PHE A 56 THR A 60 -1 O THR A 60 N GLU A 41
SHEET 3 A 4 LYS A 14 GLY A 18 -1 N VAL A 17 O GLY A 57
SHEET 4 A 4 ARG A 85 GLY A 90 -1 O ASP A 87 N PHE A 16
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes